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Database: UniProt
Entry: A0A089I1C3_9BACL
LinkDB: A0A089I1C3_9BACL
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ID   A0A089I1C3_9BACL        Unreviewed;       887 AA.
AC   A0A089I1C3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=H70357_11315 {ECO:0000313|EMBL:AIQ17182.1};
OS   Paenibacillus sp. FSL H7-0357.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ17182.1, ECO:0000313|Proteomes:UP000029508};
RN   [1] {ECO:0000313|EMBL:AIQ17182.1, ECO:0000313|Proteomes:UP000029508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ17182.1,
RC   ECO:0000313|Proteomes:UP000029508};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU004460};
CC   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC       {ECO:0000256|ARBA:ARBA00011541, ECO:0000256|RuleBase:RU004460}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; CP009241; AIQ17182.1; -; Genomic_DNA.
DR   RefSeq; WP_038588972.1; NZ_CP009241.1.
DR   AlphaFoldDB; A0A089I1C3; -.
DR   STRING; 1536774.H70357_11315; -.
DR   KEGG; paeh:H70357_11315; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_9; -.
DR   Proteomes; UP000029508; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06140; DNA_polA_I_Bacillus_like_exo; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          2..260
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          305..477
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          644..851
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   887 AA;  98566 MW;  578863E0FBADB248 CRC64;
     MDKLILIDGN NIIYRAFFAM PPLTNTAGQQ TNAVYGFTTM LLRLIEEHKP SHLIVAFDAG
     KITFRHEGYE DYKGGRQKTP PELSEQFPML KDLLRDMGVP QFEISGYEAD DIIGSISREA
     DEAGRQVMIV SGDKDMLQLA SEYTTVALVR KGVTEVELYG PQQIREKYDL TPEQIIDLKG
     LMGDASDNIP GVPGVGEKTA LKLLHQFGSV EGVLAGTGEL KGKMKEKLEE HADSAVMSKK
     LATIYREVPL EHAWEDMEFT GIKGDTAGPA LAKLEFKSLL ERLSLSAYSP SSDGAVEAVE
     AAVLDITIVG ESELEDLISA LPGISALHVE SNGENPHRAE VIGLGLSSPE RHYFVPFALL
     QSHAAAPLRA WLGDSKAPKS GYDLHRADLA LHWQGIPFAG AANDVQLAAY LLDPTEANQN
     LNDLTAKYGL PRLSPDEEVF GKGAKYKIPE LEILGNHVAR KSATVLGIVE KQQQELTETA
     MTGLFEDLEM PLSRILADME KQGIAVNKED LKELGKEFEA QISKLVAEIY EICGTEFNLN
     SPKQLGEILF VKLGLPVVKK TKTGYSTDAE VLEKLAPYHD VVRLILQYRS IAKLQSTYVE
     GLLKEVSEVT GKVHTFYRQT IAATGRLSSQ FPNLQNIPIR LEEGRKIRKV FVPSEPGWSI
     LAADYSQIEL RVLAHISGDE RMKEAFLHDM DIHTKTAMDV FGVTADQVDS NMRRSAKAVN
     FGIVYGISDY GLSQNLGISR KEASHFIEQY FEVYEGVRRY MDDIVLDARK QGYVTTLLER
     RRYLPEINAK NFNLRSFAER TAMNTPIQGT AADIIKLAMV HMDKALYERG LKSRMLLQVH
     DELVFEVPED ELELMKELLP KVMAGALKLS VPLKAEVSYG SNWYEAK
//
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